A parsimonious biophysical model correctly predicts the conserved expression stoichiometry of core bacterial mRNA translation factors, providing intuitive and quantitative design principles for in vivo pathway construction.

Analysis of the Escherichia coli DnaB helicase•bacteriophage λ helicase loader (λP) complex provides insights into helicase opening, delivery to the origin and ssDNA entry, and closing in preparation for translocation.

Coordinated regulation of co-complex members compensates for aneuploidy-induced stoichiometric imbalances in human cancer.

The mechanistic basis of molecular movement and interactions within plant root cells can be quantified using scanning fluorescence correlation spectroscopy.

Building on previous work (Pless, 2013), we argue that side-chain 'flip out' is a key event in potassium channel C-type inactivation, and propose a new method for encoding multiple noncanonical amino acids and controlling protein stoichiometry.

Fluorescence fluctuation spectroscopy is implemented for detection of up to four molecular species, allowing users to quantify molecular interactions and stoichiometry of multicomponent complexes in live cells, in a wide range of biological processes, from membrane signaling to viral assembly.

The structure of the membrane-integrated components of a unique substrate decarboxylation-driven primary-active sodium pump provides insights into its transport mechanism.

Crystal structures provide structural rationales for the transport stoichiometry of the gastric proton pump, which suffices the energy requirement for the generation of a million-fold proton gradient across the membrane.

KASH5 uses an EF-hand domain to directly interact with the light intermediate chain of dynein, promotes processive dynein motility, and facilitates dynein recruitment to the nuclear envelope during prophase I of meiosis.

A peptide toxin with therapeutic potential in stroke and pain induces multiple long-lasting conformational changes in acid-sensing ion channels and affects how the channels respond to endogenous ligands.